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Zinc in PDB 1z9g: Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan

Enzymatic activity of Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan

All present enzymatic activity of Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan:
3.4.24.27;

Protein crystallography data

The structure of Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan, PDB code: 1z9g was solved by S.L.Roderick, M.C.Fournie-Zaluski, B.P.Roques, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.000, 94.000, 132.000, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1z9g:

The structure of Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan (pdb code 1z9g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan, PDB code: 1z9g:

Zinc binding site 1 out of 1 in 1z9g

Go back to Zinc Binding Sites List in 1z9g
Zinc binding site 1 out of 1 in the Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (R)-Retro-Thiorphan within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1005

b:12.6
occ:1.00
 NE2 E:HIS146 2.0 12.6 1.0
NE2 E:HIS142 2.1 16.8 1.0
OE1 E:GLU166 2.2 17.1 1.0
SG E:RRT1006 2.3 26.1 1.0
OE2 E:GLU166 2.8 19.5 1.0
CD E:GLU166 2.8 17.0 1.0
CE1 E:HIS146 2.9 9.5 1.0
CD2 E:HIS142 3.0 11.6 1.0
CE1 E:HIS142 3.1 11.0 1.0
CD2 E:HIS146 3.1 11.9 1.0
CB2 E:RRT1006 3.5 20.0 1.0
OH E:TYR157 3.7 23.5 1.0
CA1 E:RRT1006 3.9 23.8 1.0
ND1 E:HIS146 4.1 8.9 1.0
CG E:HIS146 4.2 9.7 1.0
CG E:HIS142 4.2 7.7 1.0
ND1 E:HIS142 4.2 5.7 1.0
CG E:GLU166 4.3 8.0 1.0
NE2 E:HIS231 4.3 14.2 1.0
OE1 E:GLU143 4.5 20.6 1.0
CB E:SER169 4.6 7.2 1.0
CZ E:TYR157 4.7 23.5 1.0
CA E:GLU166 4.8 8.0 1.0
OG E:SER169 4.9 9.9 1.0
CD2 E:HIS231 4.9 19.9 1.0
N E:RRT1006 4.9 30.8 1.0
CE2 E:TYR157 4.9 24.9 1.0
O1 E:RRT1006 5.0 20.0 1.0
CB1 E:RRT1006 5.0 23.4 1.0

Reference:

S.L.Roderick, M.C.Fournie-Zaluski, B.P.Roques, B.W.Matthews. Thiorphan and Retro-Thiorphan Display Equivalent Interactions When Bound to Crystalline Thermolysin Biochemistry V. 28 1493 1989.
ISSN: ISSN 0006-2960
PubMed: 2719912
DOI: 10.1021/BI00430A011
Page generated: Wed Dec 16 03:15:26 2020

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